Research workbench
P32 of caspase-11 mutant C254A
Analyse P32 of caspase-11 mutant C254A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KMT
- Type
- protein
- Length
- 935 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-4
- EC
- 3.4.22.64
- UniProt
- P70343
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Caspase-4 (EC 3.4.22.64) | protein | 234 | 35% helix, 22% strand | P70343 |
| D | Caspase-4 (EC 3.4.22.64) | protein | 233 | 34% helix, 22% strand | P70343 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 604 | 0.78 | 0.84 | 56 | empty |
| 2 | 638 | 0.76 | 0.82 | 48 | empty |
| 3 | 434 | 0.60 | 0.76 | 40 | empty |
| 4 | 73 | 0.31 | 0.74 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1179 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1148 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 683 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P70343
- Elsewhere: RCSB PDB 6KMT · PDBe 6KMT · UniProt P70343
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